Supported by grants from the Wisconsin Milk Marketing Board and National Diary Board.
Effect of Heat Treatment and Modification on Conformation and Flavor Binding by β-Lactoglobulin
Article first published online: 25 AUG 2006
Journal of Food Science
Volume 53, Issue 3, pages 906–909, May 1988
How to Cite
O'NEILL, T. and KINSELLA, J.E. (1988), Effect of Heat Treatment and Modification on Conformation and Flavor Binding by β-Lactoglobulin. Journal of Food Science, 53: 906–909. doi: 10.1111/j.1365-2621.1988.tb08982.x
- Issue published online: 25 AUG 2006
- Article first published online: 25 AUG 2006
- Ms received 4/9/87; revised 12/14/87; accepted 12/16/87.
The flavor binding behavior of native β-lactoglobuIin (β-Lg) was significantly altered by thermal or chemical modification. Upon heat-treatment at 75°C for 10 and 20 minutes the binding affinity for 2-nonanone was reduced and the number of sites for binding was increased. This was related to conformational changes and aggregation of β-Lg. Reduction of the disulfide bonds and ethylation of carboxylic acid groups also induced conformational changes which reduced the binding affinity of β-Lg for 2-nonanone.